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(Received for publication, June 26,
1995; and in revised form, September 8, 1995) We have shown previously (Nishimura, M., Fedorov, S., and Uyeda,
K.(1994) (J. Biol. Chem. 269, 26100-26106) that the
administration of high concentrations of glucose stimulates
dephosphorylation of Fru-6-P,2-kinase:Fru-2,6-bisphosphatase in
perfused liver, and xylulose (Xu) 5-P activates the dephosphorylation
reaction. To characterize the protein phosphatase, we have purified the
Xu 5-P-activated protein phosphatase to homogeneity from livers of rats
injected with high glucose. Several protein phosphatases in the livers
were separated by DEAE-cellulose chromatography, but only one peak of
the enzyme was activated by Xu 5-P. The protein phosphatase was
inhibited by okadaic acid (IC These results
demonstrated the existence and isolation of a unique heterotrimeric
protein phosphatase 2A in rat liver which catalyzed the
dephosphorylation of Fru-6-P,2-kinase:Fru-2,6-Pase and was activated
specifically by Xu 5-P. The Xu 5-P-activated protein phosphatase 2A
explains the increased Fru 2,6-P
Volume 270,
Number 44,
Issue of November 3, 1995 pp. 26341-26346
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
= 1-3
nM) and did not require Mg
or
Ca
, suggesting that the enzyme was type 2A. The
enzyme was a heterotrimer (M
= 150,000) and
consisted of structural (A, 65 kDa), catalytic (C, 36 kDa), and
regulatory (B, 52 kDa) subunits. Amino acid sequences of five tryptic
peptides derived from the B subunit showed similarity with those of the
B
isoform of rat protein phosphatase 2A, but five out of 73
residues were different. The protein phosphatase catalyzed
dephosphorylation of Fru-6-P,2-kinase:Fru-2,6-Pase, phosphorylase a, and pyruvate kinase, and the K values were 0.8 µM, 3.7 µM, and
2.2 µM, respectively. Among these substrates
dephosphorylation of only the bifunctional enzyme was activated by Xu
5-P, and the K
value for Xu 5-P was 20
µM. Xu 5-P was the only sugar phosphate which activated
the PP2A among all the sugar phosphates examined.
level in liver after high
glucose administration.
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